Thy-1 cDNA sequence suggests a novel regulatory mechanism

Abstract

Thy-1 was originally defined in mice as a cell-surface alloantigen of thymus and brain with two allelic forms, Thy-1.1 and Thy-1.2 (ref. 1). Subsequently, the Thy-1.1 alloantigenic determinant was identified in rats². In both species, Thy-1 is present in large amounts on thymus and brain cells³ and in smaller quantities on fibroblasts⁴, epidermal cells⁵, mammary glands⁶ and immature skeletal muscle⁷. In many of these tissues the level of Thy-1 expression changes dramatically during cell differentiation. The molecules expressing the Thy-1 antigenic determinant have been isolated from rat and mouse brain cells and have been shown to have a molecular weight of 17,500 (ref. 8). One-third of the Thy-1 molecule is carbohydrate and the remainder is a polypeptide of 111 amino acids whose sequence has been fully determined⁹. We report here the isolation and characterization of a cDNA clone encoding the rat thymus Thy-1 antigen but find that the DNA sequence ends prematurely at a position corresponding to amino acid 103. It appears to be a complete transcript, however, as the last codon is followed directly by a poly(A) tract.